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P60_LISIN
ID   P60_LISIN               Reviewed;         467 AA.
AC   Q01836;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   16-NOV-2001, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Probable endopeptidase p60;
DE            EC=3.4.-.-;
DE   AltName: Full=Invasion-associated protein p60;
DE   Flags: Precursor;
GN   Name=iap; OrderedLocusNames=lin0591;
OS   Listeria innocua serovar 6a (strain ATCC BAA-680 / CLIP 11262).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=272626;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=Serovar 6b;
RX   PubMed=1514809; DOI=10.1128/aem.58.8.2625-2632.1992;
RA   Bubert A., Koehler S., Goebel W.;
RT   "The homologous and heterologous regions within the iap gene allow
RT   genus- and species-specific identification of Listeria spp. by polymerase
RT   chain reaction.";
RL   Appl. Environ. Microbiol. 58:2625-2632(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-680 / CLIP 11262;
RX   PubMed=11679669; DOI=10.1126/science.1063447;
RA   Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA   Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA   Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA   Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA   Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA   Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA   Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA   Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA   Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA   Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT   "Comparative genomics of Listeria species.";
RL   Science 294:849-852(2001).
RN   [3]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=1459966; DOI=10.1128/jb.174.24.8166-8171.1992;
RA   Bubert A., Kuhn M., Goebel W., Koehler S.;
RT   "Structural and functional properties of the p60 proteins from different
RT   Listeria species.";
RL   J. Bacteriol. 174:8166-8171(1992).
CC   -!- FUNCTION: This major extracellular protein may be involved in the
CC       invasion of non-professional phagocytic cells by Listeria.
CC   -!- DOMAIN: LysM domains are thought to be involved in peptidoglycan
CC       binding.
CC   -!- SIMILARITY: Belongs to the peptidase C40 family. {ECO:0000255|PROSITE-
CC       ProRule:PRU01284, ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAC95823.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; M80349; AAA25283.1; -; Genomic_DNA.
DR   EMBL; AL596165; CAC95823.1; ALT_INIT; Genomic_DNA.
DR   PIR; AG1506; AG1506.
DR   AlphaFoldDB; Q01836; -.
DR   STRING; 272626.lin0591; -.
DR   CAZy; CBM50; Carbohydrate-Binding Module Family 50.
DR   EnsemblBacteria; CAC95823; CAC95823; CAC95823.
DR   KEGG; lin:iap; -.
DR   eggNOG; COG0791; Bacteria.
DR   eggNOG; COG1388; Bacteria.
DR   eggNOG; COG3103; Bacteria.
DR   HOGENOM; CLU_581142_0_0_9; -.
DR   Proteomes; UP000002513; Chromosome.
DR   GO; GO:0008234; F:cysteine-type peptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd00118; LysM; 2.
DR   Gene3D; 3.10.350.10; -; 2.
DR   InterPro; IPR018392; LysM_dom.
DR   InterPro; IPR036779; LysM_dom_sf.
DR   InterPro; IPR000064; NLP_P60_dom.
DR   InterPro; IPR038765; Papain-like_cys_pep_sf.
DR   InterPro; IPR003646; SH3-like_bac-type.
DR   Pfam; PF01476; LysM; 2.
DR   Pfam; PF00877; NLPC_P60; 1.
DR   Pfam; PF08239; SH3_3; 1.
DR   SMART; SM00257; LysM; 2.
DR   SMART; SM00287; SH3b; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   SUPFAM; SSF54106; SSF54106; 2.
DR   PROSITE; PS51782; LYSM; 2.
DR   PROSITE; PS51935; NLPC_P60; 1.
DR   PROSITE; PS51781; SH3B; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Protease; Repeat; Signal; Thiol protease.
FT   SIGNAL          1..27
FT                   /evidence="ECO:0000250"
FT   CHAIN           28..467
FT                   /note="Probable endopeptidase p60"
FT                   /id="PRO_0000019758"
FT   DOMAIN          28..71
FT                   /note="LysM 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          79..143
FT                   /note="SH3b"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01117"
FT   DOMAIN          199..242
FT                   /note="LysM 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01118"
FT   DOMAIN          349..467
FT                   /note="NlpC/P60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   REGION          154..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          247..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          330..343
FT                   /note="7 X 2 AA tandem repeats of T-N"
FT   COMPBIAS        162..183
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        268..348
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        379
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        429
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   ACT_SITE        441
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01284"
FT   VARIANT         240
FT                   /note="L -> P (in strain: Serovar 6B)"
FT   VARIANT         328
FT                   /note="K -> KNTNTNTNTNTNTNT (in strain: Serovar 6B)"
SQ   SEQUENCE   467 AA;  49044 MW;  0F40B031BD2175C1 CRC64;
     MNMKKATIAA TAGIAVTAFA APTIASASTV VVEAGDTLWG IAQSKGTTVD AIKKANNLTT
     DKIVPGQKLQ VNEVATEEKA EKSVSATWLN VRSGAGVDHS ILTSIKGGTK VTVETTESNG
     WHKITYNDGK TGYVNGKYLT DKATSTPVVK QEVKKETTQQ VKPATEAKTE VKQPTTQQTA
     PAPKAAETKE APVVDQNATT HNVKSGDTIW ALSVKYGVSV QDIMSWNNLS SSSIYVGQKL
     AIKQPTKTVA PKAETKTQAP AAEKQTAPAV KENSNANTAT TEKKETATEQ QTTTKAPTQA
     AKPAPAPSTN TNKTNTTNNN TNASTPSKNT NTNTNTNTNT NTNQGSTNNA SASALIAEAQ
     KHLGKAYSWG GNGPTTFDCS GFTKYVFAKS GISLPRTSGA QYASTTRISE SQAKPGDLVF
     FDYGSGISHV GIYVGNGQMI NAQDNGVKYD NIHGAGWGKF LVGFGRV
 
 
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